Q570Y9 · DPTOR_MOUSE

  • Protein
    DEP domain-containing mTOR-interacting protein
  • Gene
    Deptor
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes. DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy. In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity.

Activity regulation

Inhibited upon phosphatidic acid-binding: phosphatidic acid produced upon mitogenic stimulation promotes DEPTOR dissociatiom from the mTORC1 and mTORC2 complexes, leading to their activation. Specifically binds unsaturated phosphatidic acid, such as 16:0-18:1, 18:0-18:1 and di-18:1. Inhibited when nutrients are present via a feedback loop: phosphorylation by MTOR promotes DEPTOR ubiquitination and degradation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentlysosomal membrane
Molecular Functionphosphatidic acid binding
Molecular Functionprotein kinase inhibitor activity
Molecular Functionprotein serine/threonine kinase inhibitor activity
Biological Processintracellular signal transduction
Biological Processnegative regulation of cell size
Biological Processnegative regulation of TORC1 signaling
Biological Processnegative regulation of TORC2 signaling
Biological Processpositive regulation of autophagy
Biological Processregulation of extrinsic apoptotic signaling pathway

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    DEP domain-containing mTOR-interacting protein
  • Alternative names
    • DEP domain-containing protein 6

Gene names

    • Name
      Deptor
    • Synonyms
      Depdc6, Kiaa4200

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q570Y9
  • Secondary accessions
    • Q3UM00
    • Q3UT08

Proteomes

Organism-specific databases

Subcellular Location

Lysosome membrane
Note: Localizes to the lysosomal membrane when associated with the mTORC1 and mTORC2 complexes.

Keywords

PTM/Processing

Features

Showing features for modified residue, chain.

TypeIDPosition(s)Description
Modified residue1N-acetylmethionine
ChainPRO_00002847851-409DEP domain-containing mTOR-interacting protein
Modified residue235Phosphoserine
Modified residue241Phosphothreonine
Modified residue244Phosphoserine
Modified residue258Phosphoserine
Modified residue259Phosphothreonine
Modified residue263Phosphoserine
Modified residue265Phosphoserine
Modified residue280Phosphoserine
Modified residue282Phosphoserine
Modified residue283Phosphoserine
Modified residue286Phosphoserine
Modified residue287Phosphoserine
Modified residue289Phosphotyrosine
Modified residue291Phosphoserine
Modified residue293Phosphoserine
Modified residue295Phosphothreonine
Modified residue297Phosphoserine
Modified residue298Phosphoserine
Modified residue299Phosphoserine

Post-translational modification

Phosphorylation weakens interaction with MTOR within mTORC1 and mTORC2 (By similarity).
Phosphorylated at Ser-286, Ser-287 and Ser-291 in response to mitogenic stimulation by MTOR: DEPTOR is either directly phosphorylated by MTOR or indirectly via proteins kinases that are activated by MTOR, such as CK1/CSNK1A1 (By similarity).
Phosphorylation at Ser-286, Ser-287 and Ser-291 promotes ubiquitination by the SCF(BTRC) complex, followed by degradation (By similarity).
Phosphorylation at Ser-235 by MAPK3/ERK1 promotes deubiquitination by USP7, enhancing its stability (By similarity).
Phosphorylation at Tyr-291 by SYK impairs its interaction with MTOR, promoting mTORC1 and mTORC2 signaling (By similarity).
Ubiquitinated; leading to proteasomal degradation (By similarity).
Ubiquitination by the SCF(BTRC) and SCF(FBXW11) complexes following phosphorylation at Ser-286, Ser-287 and Ser-291 by MTOR, leads to its degradation by the proteasome (By similarity).
Deubiquitinated by OTUB1 in response to amino acid via a non-canonical mechanism, leading to DEPTOR stability (By similarity).
Deubiquitinated by USP7 following phosphorylation at Ser-235, promoting its stability (By similarity).

Keywords

Proteomic databases

PTM databases

Expression

Developmental stage

At postnatal day 1 (P1), in cartilage growth plate, primarily expressed in resting and proliferating chondrocytes. This expression pattern is maintained at least until P21 (at protein level).

Gene expression databases

Interaction

Subunit

Associated component of the mechanistic target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8 and RPTOR. Associated component of the mechanistic target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and DEPTOR. Interacts (via PDZ domain) with MTOR; interacts with MTOR within both mTORC1 and mTORC2. Interacts (via PDZ domain) with MINAR1 (via N-terminus). Interacts with SIK3.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, motif.

TypeIDPosition(s)Description
Compositional bias1-21Polar residues
Region1-23Disordered
Domain36-119DEP 1
Domain146-219DEP 2
Motif217-235DDEX motif
Motif286-291BetaTrCP degron motif
Domain330-407PDZ

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q570Y9-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    409
  • Mass (Da)
    46,120
  • Last updated
    2007-04-17 v2
  • Checksum
    072062418DADDF8E
MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFALDSEVKAFMRGQRLYEKLMSPETTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMDHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNETSPSSQETHDSPFCLRKQSHDSRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELDC

Q570Y9-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-40: MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQL → MKQAFLVVLRHSISEDRLPPLSVITSGC

Q570Y9-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 368-409: VCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELDC → DTGTESRKIVTSRLAWATWQDLMGGKVGGDAIPI

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2I3BRE1A0A2I3BRE1_MOUSEDeptor100
B2ZRS5B2ZRS5_MOUSEDeptor401

Sequence caution

The sequence BAD90225.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Compositional bias1-21Polar residues
Alternative sequenceVSP_0246481-40in isoform 2
Sequence conflict11in Ref. 2; BAE26298
Sequence conflict125in Ref. 2; BAE26298
Sequence conflict128in Ref. 2; BAE26298
Sequence conflict149in Ref. 2; BAE26298
Alternative sequenceVSP_024649368-409in isoform 3

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK220300
EMBL· GenBank· DDBJ
BAD90225.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK139888
EMBL· GenBank· DDBJ
BAE24172.1
EMBL· GenBank· DDBJ
mRNA
AK145208
EMBL· GenBank· DDBJ
BAE26298.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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